PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 23699518-1 2013 Spinocerebellar ataxia 17 (SCA17) is an autosomal-dominant, late-onset neurodegenerative disorder caused by an expanded polyglutamine (polyQ) repeat in the TATA-box-binding protein (TBP). polyglutamine 120-133 ataxin 7 Homo sapiens 27-32 23699518-1 2013 Spinocerebellar ataxia 17 (SCA17) is an autosomal-dominant, late-onset neurodegenerative disorder caused by an expanded polyglutamine (polyQ) repeat in the TATA-box-binding protein (TBP). polyglutamine 135-140 ataxin 7 Homo sapiens 27-32 22367614-1 2012 Spinocerebellar ataxia type 7 (SCA7) is one of nine neurodegenerative disorders caused by expanded polyglutamine repeats, and a common toxic gain-of-function mechanism has been proposed. polyglutamine 99-112 ataxin 7 Homo sapiens 0-29 22684686-6 2012 Recent findings show that the brain is commonly seriously affected in the polyglutamine SCAs (i.e. SCA1, SCA2, SCA3, SCA6, SCA7, and SCA17) and that the patterns of brain damage in these diseases overlap considerably in patients suffering from advanced disease stages. polyglutamine 74-87 ataxin 7 Homo sapiens 123-127 22684686-6 2012 Recent findings show that the brain is commonly seriously affected in the polyglutamine SCAs (i.e. SCA1, SCA2, SCA3, SCA6, SCA7, and SCA17) and that the patterns of brain damage in these diseases overlap considerably in patients suffering from advanced disease stages. polyglutamine 74-87 ataxin 7 Homo sapiens 133-138 23236151-0 2012 Reelin is a target of polyglutamine expanded ataxin-7 in human spinocerebellar ataxia type 7 (SCA7) astrocytes. polyglutamine 22-35 ataxin 7 Homo sapiens 45-53 23236151-0 2012 Reelin is a target of polyglutamine expanded ataxin-7 in human spinocerebellar ataxia type 7 (SCA7) astrocytes. polyglutamine 22-35 ataxin 7 Homo sapiens 63-92 23236151-0 2012 Reelin is a target of polyglutamine expanded ataxin-7 in human spinocerebellar ataxia type 7 (SCA7) astrocytes. polyglutamine 22-35 ataxin 7 Homo sapiens 94-98 23236151-1 2012 Spinocerebellar ataxia type 7 (SCA7) is an autosomal-dominant neurodegenerative disorder that results from polyglutamine expansion of the ataxin-7 (ATXN7) protein. polyglutamine 107-120 ataxin 7 Homo sapiens 0-29 23236151-1 2012 Spinocerebellar ataxia type 7 (SCA7) is an autosomal-dominant neurodegenerative disorder that results from polyglutamine expansion of the ataxin-7 (ATXN7) protein. polyglutamine 107-120 ataxin 7 Homo sapiens 31-35 23236151-1 2012 Spinocerebellar ataxia type 7 (SCA7) is an autosomal-dominant neurodegenerative disorder that results from polyglutamine expansion of the ataxin-7 (ATXN7) protein. polyglutamine 107-120 ataxin 7 Homo sapiens 138-146 23236151-1 2012 Spinocerebellar ataxia type 7 (SCA7) is an autosomal-dominant neurodegenerative disorder that results from polyglutamine expansion of the ataxin-7 (ATXN7) protein. polyglutamine 107-120 ataxin 7 Homo sapiens 148-153 23236151-5 2012 We found that polyglutamine expansion decreased ATXN7 occupancy, which correlated with increased levels of histone H2B monoubiquitination, at the reelin promoter. polyglutamine 14-27 ataxin 7 Homo sapiens 48-53 22827889-1 2012 BACKGROUND: Spinocerebellar ataxia type 7 (SCA7) is one of nine inherited neurodegenerative disorders caused by polyglutamine (polyQ) expansions. polyglutamine 112-125 ataxin 7 Homo sapiens 12-41 22827889-1 2012 BACKGROUND: Spinocerebellar ataxia type 7 (SCA7) is one of nine inherited neurodegenerative disorders caused by polyglutamine (polyQ) expansions. polyglutamine 112-125 ataxin 7 Homo sapiens 43-47 22827889-1 2012 BACKGROUND: Spinocerebellar ataxia type 7 (SCA7) is one of nine inherited neurodegenerative disorders caused by polyglutamine (polyQ) expansions. polyglutamine 127-132 ataxin 7 Homo sapiens 12-41 22827889-1 2012 BACKGROUND: Spinocerebellar ataxia type 7 (SCA7) is one of nine inherited neurodegenerative disorders caused by polyglutamine (polyQ) expansions. polyglutamine 127-132 ataxin 7 Homo sapiens 43-47 22827889-4 2012 RESULTS: In this study we show that expression of polyQ expanded ATXN7 in a novel stable inducible cell model first results in a concomitant increase in ROS levels and aggregation of the disease protein and later cellular toxicity. polyglutamine 50-55 ataxin 7 Homo sapiens 65-70 22367614-1 2012 Spinocerebellar ataxia type 7 (SCA7) is one of nine neurodegenerative disorders caused by expanded polyglutamine repeats, and a common toxic gain-of-function mechanism has been proposed. polyglutamine 99-112 ataxin 7 Homo sapiens 31-35 22664922-2 2012 The expansion of a polyglutamine repeat in the TATA binding protein (TBP) causes a neurodegenerative disease, Spinocerebellar Ataxia 17 (SCA17). polyglutamine 19-32 ataxin 7 Homo sapiens 110-135 22664922-2 2012 The expansion of a polyglutamine repeat in the TATA binding protein (TBP) causes a neurodegenerative disease, Spinocerebellar Ataxia 17 (SCA17). polyglutamine 19-32 ataxin 7 Homo sapiens 137-142 20732423-1 2011 In spinocerebellar ataxia-7 (SCA7), a polyglutamine (polyQ) expansion in the ataxin-7 protein leads to the formation of neuronal intranuclear inclusions (NIIs) and neurodegeneration. polyglutamine 38-51 ataxin 7 Homo sapiens 3-27 21653638-1 2011 Expanded polyglutamine (polyQ) tract in the human TATA-box-binding protein (hTBP) causes the neurodegenerative disease spinocerebellar ataxia 17 (SCA17). polyglutamine 9-22 ataxin 7 Homo sapiens 146-151 21653638-1 2011 Expanded polyglutamine (polyQ) tract in the human TATA-box-binding protein (hTBP) causes the neurodegenerative disease spinocerebellar ataxia 17 (SCA17). polyglutamine 24-29 ataxin 7 Homo sapiens 146-151 21653638-2 2011 To investigate the pathological effects of polyQ expansion, we established a SCA17 model in Drosophila. polyglutamine 43-48 ataxin 7 Homo sapiens 77-82 21078624-1 2011 Spinocerebellar ataxias 6 and 7 (SCA6 and SCA7) are neurodegenerative disorders caused by expansion of CAG repeats encoding polyglutamine (polyQ) tracts in CACNA1A, the alpha1A subunit of the P/Q-type calcium channel, and ataxin-7 (ATXN7), a component of a chromatin-remodeling complex, respectively. polyglutamine 124-137 ataxin 7 Homo sapiens 42-46 21078624-1 2011 Spinocerebellar ataxias 6 and 7 (SCA6 and SCA7) are neurodegenerative disorders caused by expansion of CAG repeats encoding polyglutamine (polyQ) tracts in CACNA1A, the alpha1A subunit of the P/Q-type calcium channel, and ataxin-7 (ATXN7), a component of a chromatin-remodeling complex, respectively. polyglutamine 139-144 ataxin 7 Homo sapiens 42-46 21078624-1 2011 Spinocerebellar ataxias 6 and 7 (SCA6 and SCA7) are neurodegenerative disorders caused by expansion of CAG repeats encoding polyglutamine (polyQ) tracts in CACNA1A, the alpha1A subunit of the P/Q-type calcium channel, and ataxin-7 (ATXN7), a component of a chromatin-remodeling complex, respectively. polyglutamine 139-144 ataxin 7 Homo sapiens 222-230 21078624-1 2011 Spinocerebellar ataxias 6 and 7 (SCA6 and SCA7) are neurodegenerative disorders caused by expansion of CAG repeats encoding polyglutamine (polyQ) tracts in CACNA1A, the alpha1A subunit of the P/Q-type calcium channel, and ataxin-7 (ATXN7), a component of a chromatin-remodeling complex, respectively. polyglutamine 139-144 ataxin 7 Homo sapiens 232-237 20732423-1 2011 In spinocerebellar ataxia-7 (SCA7), a polyglutamine (polyQ) expansion in the ataxin-7 protein leads to the formation of neuronal intranuclear inclusions (NIIs) and neurodegeneration. polyglutamine 38-51 ataxin 7 Homo sapiens 29-33 20732423-1 2011 In spinocerebellar ataxia-7 (SCA7), a polyglutamine (polyQ) expansion in the ataxin-7 protein leads to the formation of neuronal intranuclear inclusions (NIIs) and neurodegeneration. polyglutamine 38-51 ataxin 7 Homo sapiens 77-85 20732423-1 2011 In spinocerebellar ataxia-7 (SCA7), a polyglutamine (polyQ) expansion in the ataxin-7 protein leads to the formation of neuronal intranuclear inclusions (NIIs) and neurodegeneration. polyglutamine 53-58 ataxin 7 Homo sapiens 3-27 20732423-1 2011 In spinocerebellar ataxia-7 (SCA7), a polyglutamine (polyQ) expansion in the ataxin-7 protein leads to the formation of neuronal intranuclear inclusions (NIIs) and neurodegeneration. polyglutamine 53-58 ataxin 7 Homo sapiens 29-33 20732423-1 2011 In spinocerebellar ataxia-7 (SCA7), a polyglutamine (polyQ) expansion in the ataxin-7 protein leads to the formation of neuronal intranuclear inclusions (NIIs) and neurodegeneration. polyglutamine 53-58 ataxin 7 Homo sapiens 77-85 19843541-0 2010 SUMOylation attenuates the aggregation propensity and cellular toxicity of the polyglutamine expanded ataxin-7. polyglutamine 79-92 ataxin 7 Homo sapiens 102-110 19843541-2 2010 Spinocerebellar ataxia type 7 (SCA7) is a neurodegenerative disorder, whose pathology is caused by an expansion of a polyglutamine stretch in the protein ataxin-7 (ATXN7). polyglutamine 117-130 ataxin 7 Homo sapiens 0-29 19843541-2 2010 Spinocerebellar ataxia type 7 (SCA7) is a neurodegenerative disorder, whose pathology is caused by an expansion of a polyglutamine stretch in the protein ataxin-7 (ATXN7). polyglutamine 117-130 ataxin 7 Homo sapiens 31-35 19843541-2 2010 Spinocerebellar ataxia type 7 (SCA7) is a neurodegenerative disorder, whose pathology is caused by an expansion of a polyglutamine stretch in the protein ataxin-7 (ATXN7). polyglutamine 117-130 ataxin 7 Homo sapiens 154-162 19843541-2 2010 Spinocerebellar ataxia type 7 (SCA7) is a neurodegenerative disorder, whose pathology is caused by an expansion of a polyglutamine stretch in the protein ataxin-7 (ATXN7). polyglutamine 117-130 ataxin 7 Homo sapiens 164-169 19955365-2 2009 Proteolytic processing of ataxin-7 by caspase-7 generates N-terminal toxic polyQ-containing fragments that accumulate with disease progression and play an important role in SCA7 pathogenesis. polyglutamine 75-80 ataxin 7 Homo sapiens 173-177 19955365-1 2009 Polyglutamine (polyQ) expansion within the ataxin-7 protein, a member of the STAGA [SPT3-TAF(II)31-GCN5L acetylase] and TFTC (GCN5 and TRRAP) chromatin remodeling complexes, causes the neurodegenerative disease spinocerebellar ataxia type 7 (SCA7). polyglutamine 0-13 ataxin 7 Homo sapiens 43-51 19955365-1 2009 Polyglutamine (polyQ) expansion within the ataxin-7 protein, a member of the STAGA [SPT3-TAF(II)31-GCN5L acetylase] and TFTC (GCN5 and TRRAP) chromatin remodeling complexes, causes the neurodegenerative disease spinocerebellar ataxia type 7 (SCA7). polyglutamine 0-13 ataxin 7 Homo sapiens 242-246 19955365-1 2009 Polyglutamine (polyQ) expansion within the ataxin-7 protein, a member of the STAGA [SPT3-TAF(II)31-GCN5L acetylase] and TFTC (GCN5 and TRRAP) chromatin remodeling complexes, causes the neurodegenerative disease spinocerebellar ataxia type 7 (SCA7). polyglutamine 15-20 ataxin 7 Homo sapiens 43-51 19955365-1 2009 Polyglutamine (polyQ) expansion within the ataxin-7 protein, a member of the STAGA [SPT3-TAF(II)31-GCN5L acetylase] and TFTC (GCN5 and TRRAP) chromatin remodeling complexes, causes the neurodegenerative disease spinocerebellar ataxia type 7 (SCA7). polyglutamine 15-20 ataxin 7 Homo sapiens 242-246 19955365-2 2009 Proteolytic processing of ataxin-7 by caspase-7 generates N-terminal toxic polyQ-containing fragments that accumulate with disease progression and play an important role in SCA7 pathogenesis. polyglutamine 75-80 ataxin 7 Homo sapiens 26-34 18418675-1 2008 Spinocerebellar ataxia type 7 (SCA7) is unique among CAG/polyglutamine (polyQ) repeat diseases due to dramatic intergenerational instability in repeat length and an associated cone-rod dystrophy retinal degeneration phenotype. polyglutamine 57-70 ataxin 7 Homo sapiens 0-29 20030245-3 2009 These "polyglutamine disorders" are, SCA1, SCA2, Machado-Joseph disease, SCA6, SCA7, SCA17 and DRPLA. polyglutamine 7-20 ataxin 7 Homo sapiens 79-83 20030245-3 2009 These "polyglutamine disorders" are, SCA1, SCA2, Machado-Joseph disease, SCA6, SCA7, SCA17 and DRPLA. polyglutamine 7-20 ataxin 7 Homo sapiens 85-90 17971076-1 2008 Spinocerebellar ataxia type 7 (SCA7) represents a rare and severe autosomal dominantly inherited ataxic disorder and is among the known CAG-repeat, or polyglutamine, diseases. polyglutamine 151-164 ataxin 7 Homo sapiens 0-29 17971076-1 2008 Spinocerebellar ataxia type 7 (SCA7) represents a rare and severe autosomal dominantly inherited ataxic disorder and is among the known CAG-repeat, or polyglutamine, diseases. polyglutamine 151-164 ataxin 7 Homo sapiens 31-35 18043721-5 2008 SCA17 is a typical polyglutamine disease caused by CAG repeat expansion in TBP (TATA binding protein), and is unique in that the pure expanded polyglutamine tract is coded by either a simple configuration with long stretches of pure CAGs or a complex configuration containing CAA interruptions. polyglutamine 19-32 ataxin 7 Homo sapiens 0-5 18418675-1 2008 Spinocerebellar ataxia type 7 (SCA7) is unique among CAG/polyglutamine (polyQ) repeat diseases due to dramatic intergenerational instability in repeat length and an associated cone-rod dystrophy retinal degeneration phenotype. polyglutamine 57-70 ataxin 7 Homo sapiens 31-35 18418675-1 2008 Spinocerebellar ataxia type 7 (SCA7) is unique among CAG/polyglutamine (polyQ) repeat diseases due to dramatic intergenerational instability in repeat length and an associated cone-rod dystrophy retinal degeneration phenotype. polyglutamine 72-77 ataxin 7 Homo sapiens 0-29 18418675-1 2008 Spinocerebellar ataxia type 7 (SCA7) is unique among CAG/polyglutamine (polyQ) repeat diseases due to dramatic intergenerational instability in repeat length and an associated cone-rod dystrophy retinal degeneration phenotype. polyglutamine 72-77 ataxin 7 Homo sapiens 31-35 18418675-2 2008 SCA7 is caused by a polyQ expansion in the protein ataxin-7. polyglutamine 20-25 ataxin 7 Homo sapiens 0-4 18418675-2 2008 SCA7 is caused by a polyQ expansion in the protein ataxin-7. polyglutamine 20-25 ataxin 7 Homo sapiens 51-59 18418675-4 2008 Several potential mechanisms for the molecular pathogenesis of polyQ-expanded ataxin-7 have been suggested. polyglutamine 63-68 ataxin 7 Homo sapiens 78-86 18418675-5 2008 These include, but are not limited to, alteration of endogenous ataxin-7 function, abnormal processing and stability of polyQ ataxin-7, and alteration of transcriptional regulation via interaction of polyQ-expanded ataxin-7 with other transcriptional regulators. polyglutamine 120-125 ataxin 7 Homo sapiens 126-134 18418675-5 2008 These include, but are not limited to, alteration of endogenous ataxin-7 function, abnormal processing and stability of polyQ ataxin-7, and alteration of transcriptional regulation via interaction of polyQ-expanded ataxin-7 with other transcriptional regulators. polyglutamine 120-125 ataxin 7 Homo sapiens 126-134 18418675-7 2008 PolyQ-expanded ataxin-7 can cause non-cell autonomous neurodegeneration in cerebellar Purkinje cells. polyglutamine 0-5 ataxin 7 Homo sapiens 15-23 18418687-1 2008 Spinocerebellar ataxia 17 (SCA17) or Huntington"s disease-like-4 is a neurodegenerative disease caused by the expansion above 44 units of a CAG/CAA repeat in the coding region of the TATA box binding protein (TBP) gene leading to an abnormal expansion of a polyglutamine stretch in the corresponding protein. polyglutamine 257-270 ataxin 7 Homo sapiens 0-25 18418687-1 2008 Spinocerebellar ataxia 17 (SCA17) or Huntington"s disease-like-4 is a neurodegenerative disease caused by the expansion above 44 units of a CAG/CAA repeat in the coding region of the TATA box binding protein (TBP) gene leading to an abnormal expansion of a polyglutamine stretch in the corresponding protein. polyglutamine 257-270 ataxin 7 Homo sapiens 27-32 17868456-1 2007 BACKGROUND: Huntington"s disease, spinal and bulbar muscular atrophy, and spinocerebellar ataxia 17 (SCA17) are caused by expansions in the polyglutamine (polyQ) repeats in Huntingtin protein (Htt), androgen receptor protein (AR), and TATA-binding protein (TBP), respectively. polyglutamine 140-153 ataxin 7 Homo sapiens 74-99 17646170-6 2007 Although ataxin-7 displays toxicity, forms nuclear aggregates, and represses transcription in human embryonic kidney 293T cells in a polyQ length-dependent manner, expression of the non-cleavable D266N/D344N form of polyQ-expanded ataxin-7 attenuated cell death, aggregate formation, and transcriptional interference. polyglutamine 133-138 ataxin 7 Homo sapiens 9-17 17994014-1 2007 Expansion of the polyglutamine (polyQ) tract in human TATA-box binding protein (TBP) causes the neurodegenerative disease spinocerebellar ataxia 17 (SCA17). polyglutamine 17-30 ataxin 7 Homo sapiens 149-154 17994014-1 2007 Expansion of the polyglutamine (polyQ) tract in human TATA-box binding protein (TBP) causes the neurodegenerative disease spinocerebellar ataxia 17 (SCA17). polyglutamine 32-37 ataxin 7 Homo sapiens 149-154 17868456-1 2007 BACKGROUND: Huntington"s disease, spinal and bulbar muscular atrophy, and spinocerebellar ataxia 17 (SCA17) are caused by expansions in the polyglutamine (polyQ) repeats in Huntingtin protein (Htt), androgen receptor protein (AR), and TATA-binding protein (TBP), respectively. polyglutamine 140-153 ataxin 7 Homo sapiens 101-106 17868456-1 2007 BACKGROUND: Huntington"s disease, spinal and bulbar muscular atrophy, and spinocerebellar ataxia 17 (SCA17) are caused by expansions in the polyglutamine (polyQ) repeats in Huntingtin protein (Htt), androgen receptor protein (AR), and TATA-binding protein (TBP), respectively. polyglutamine 155-160 ataxin 7 Homo sapiens 74-99 17868456-1 2007 BACKGROUND: Huntington"s disease, spinal and bulbar muscular atrophy, and spinocerebellar ataxia 17 (SCA17) are caused by expansions in the polyglutamine (polyQ) repeats in Huntingtin protein (Htt), androgen receptor protein (AR), and TATA-binding protein (TBP), respectively. polyglutamine 155-160 ataxin 7 Homo sapiens 101-106 16962040-0 2006 [Role of chromatin alterations in neurodegeneration induced by polyglutamine-expanded ataxin-7]. polyglutamine 63-76 ataxin 7 Homo sapiens 86-94 17005371-0 2007 Polyglutamine-expanded ataxin-7 decreases nuclear translocation of NF-kappaB p65 and impairs NF-kappaB activity by inhibiting proteasome activity of cerebellar neurons. polyglutamine 0-13 ataxin 7 Homo sapiens 23-31 17005371-1 2007 Our recent study indicated that polyglutamine-expanded ataxin-7-Q75 induced apoptotic death of cultured cerebellar neurons by downregulating Bcl-x(L) expression and activating mitochondrial apoptotic cascade. polyglutamine 32-45 ataxin 7 Homo sapiens 55-63 17005371-11 2007 Our study provides the evidence that polyglutamine-expanded ataxin-7-Q75 decreases nuclear translocation of NF-kappaB p65 and impairs NF-kappaB activity by inhibiting proteasome activity of cerebellar neurons. polyglutamine 37-50 ataxin 7 Homo sapiens 60-68 17344386-1 2007 Spinocerebellar ataxia 7 (SCA7) is a neurodegenerative disease caused by a polyglutamine (polyQ) expansion in the ataxin 7 (ATXN7) protein, a member of a multiprotein complex involved in histone acetylation. polyglutamine 75-88 ataxin 7 Homo sapiens 26-30 17344386-1 2007 Spinocerebellar ataxia 7 (SCA7) is a neurodegenerative disease caused by a polyglutamine (polyQ) expansion in the ataxin 7 (ATXN7) protein, a member of a multiprotein complex involved in histone acetylation. polyglutamine 90-95 ataxin 7 Homo sapiens 26-30 17344386-2 2007 We have created a conditional Drosophila model of SCA7 in which expression of truncated ATXN7 (ATXN7T) with a pathogenic polyQ expansion is induced in neurons in adult flies. polyglutamine 121-126 ataxin 7 Homo sapiens 50-54 15964171-0 2006 Polyglutamine-expanded ataxin-7 activates mitochondrial apoptotic pathway of cerebellar neurons by upregulating Bax and downregulating Bcl-x(L). polyglutamine 0-13 ataxin 7 Homo sapiens 23-31 15964171-1 2006 Spinocerebellar ataxia type 7 (SCA7) is an autosomal dominant neurodegenerative disorder caused by polyglutamine-expanded ataxin-7. polyglutamine 99-112 ataxin 7 Homo sapiens 0-29 15964171-1 2006 Spinocerebellar ataxia type 7 (SCA7) is an autosomal dominant neurodegenerative disorder caused by polyglutamine-expanded ataxin-7. polyglutamine 99-112 ataxin 7 Homo sapiens 31-35 15964171-1 2006 Spinocerebellar ataxia type 7 (SCA7) is an autosomal dominant neurodegenerative disorder caused by polyglutamine-expanded ataxin-7. polyglutamine 99-112 ataxin 7 Homo sapiens 122-130 15964171-4 2006 TUNEL staining studies indicated that polyglutamine-expanded ataxin-7-Q75 caused apoptotic cell death of cultured cerebellar neurons. polyglutamine 38-51 ataxin 7 Homo sapiens 61-69 15964171-6 2006 Polyglutamine-expanded ataxin-7-Q75 promoted the release of apoptogenic cytochrome-c and Smac from mitochondria, which was preceded by the downregulation of Bcl-x(L) protein and upregulation of Bax protein expression in cultured cerebellar neurons. polyglutamine 0-13 ataxin 7 Homo sapiens 23-31 15964171-8 2006 The present study provides the evidence that polyglutamine-expanded ataxin-7-Q75 activates mitochondria-mediated apoptotic cascade and induces neuronal death by upregulating Bax expression and downregulating Bcl-x(L) expression of cerebellar neurons. polyglutamine 45-58 ataxin 7 Homo sapiens 68-76 16314424-6 2006 Subtle point mutation of the NES in polyglutamine expanded ataxin-7 increased toxicity in primary cerebellar neurons in a polyglutamine length-dependent manner in the context of full-length ataxin-7. polyglutamine 36-49 ataxin 7 Homo sapiens 59-67 16325416-0 2006 Polyglutamine and polyalanine expansions in ataxin7 result in different types of aggregation and levels of toxicity. polyglutamine 0-13 ataxin 7 Homo sapiens 44-51 16325416-1 2006 Spinocerebellar ataxia type 7 (SCA7) is caused by expansion of a (CAG)n repeat in the ataxin7 gene, resulting in an abnormally long polyglutamine polyQ tract in the translated protein that aggregates in the form of neuronal intranuclear inclusions. polyglutamine 132-145 ataxin 7 Homo sapiens 0-29 16325416-1 2006 Spinocerebellar ataxia type 7 (SCA7) is caused by expansion of a (CAG)n repeat in the ataxin7 gene, resulting in an abnormally long polyglutamine polyQ tract in the translated protein that aggregates in the form of neuronal intranuclear inclusions. polyglutamine 132-145 ataxin 7 Homo sapiens 31-35 16325416-1 2006 Spinocerebellar ataxia type 7 (SCA7) is caused by expansion of a (CAG)n repeat in the ataxin7 gene, resulting in an abnormally long polyglutamine polyQ tract in the translated protein that aggregates in the form of neuronal intranuclear inclusions. polyglutamine 132-145 ataxin 7 Homo sapiens 86-93 16314424-1 2006 Spinocerebellar ataxia type 7 is a progressive neurodegenerative disorder caused by a CAG DNA triplet repeat expansion leading to an expanded polyglutamine tract in the ataxin-7 protein. polyglutamine 142-155 ataxin 7 Homo sapiens 169-177 16314424-5 2006 Polyglutamine expansion was seen to reduce the nuclear export rate of mutant ataxin-7 relative to wild-type ataxin-7. polyglutamine 0-13 ataxin 7 Homo sapiens 77-85 16314424-6 2006 Subtle point mutation of the NES in polyglutamine expanded ataxin-7 increased toxicity in primary cerebellar neurons in a polyglutamine length-dependent manner in the context of full-length ataxin-7. polyglutamine 36-49 ataxin 7 Homo sapiens 190-198 16314424-6 2006 Subtle point mutation of the NES in polyglutamine expanded ataxin-7 increased toxicity in primary cerebellar neurons in a polyglutamine length-dependent manner in the context of full-length ataxin-7. polyglutamine 122-135 ataxin 7 Homo sapiens 59-67 16626296-0 2006 Both normal and polyglutamine- expanded ataxin-7 are components of TFTC-type GCN5 histone acetyltransferase- containing complexes. polyglutamine 16-29 ataxin 7 Homo sapiens 40-48 16626296-5 2006 Moreover, polyglutamine expansion in ataxin-7 did not affect its incorporation into TFTCs/STAGA complexes purified from cells from a SCA7 patient. polyglutamine 10-23 ataxin 7 Homo sapiens 37-45 15936949-2 2005 The disease is caused by a polyglutamine expansion in ataxin-7, a protein found in two complexes TFTC and STAGA, involved in transcriptional regulation. polyglutamine 27-40 ataxin 7 Homo sapiens 54-62 15989694-1 2005 BACKGROUND: Spinocerebellar ataxia type 17 (SCA17), a neurodegenerative disorder in man, is caused by an expanded polymorphic polyglutamine-encoding trinucleotide repeat in the gene for TATA-box binding protein (TBP), a main transcription factor. polyglutamine 126-139 ataxin 7 Homo sapiens 12-42 15989694-1 2005 BACKGROUND: Spinocerebellar ataxia type 17 (SCA17), a neurodegenerative disorder in man, is caused by an expanded polymorphic polyglutamine-encoding trinucleotide repeat in the gene for TATA-box binding protein (TBP), a main transcription factor. polyglutamine 126-139 ataxin 7 Homo sapiens 44-49 15932940-0 2005 Polyglutamine-expanded ataxin-7 inhibits STAGA histone acetyltransferase activity to produce retinal degeneration. polyglutamine 0-13 ataxin 7 Homo sapiens 23-31 15932941-3 2005 Here, we identify the protein Sgf73/Sca7 as a component of SAGA and SLIK, and a homologue of the human SCA7-encoded protein ataxin-7, which, in its polyglutamine expanded pathological form, is responsible for the neurodegenerative disease spinocerebellar ataxia 7 (SCA7). polyglutamine 148-161 ataxin 7 Homo sapiens 103-107 15932941-3 2005 Here, we identify the protein Sgf73/Sca7 as a component of SAGA and SLIK, and a homologue of the human SCA7-encoded protein ataxin-7, which, in its polyglutamine expanded pathological form, is responsible for the neurodegenerative disease spinocerebellar ataxia 7 (SCA7). polyglutamine 148-161 ataxin 7 Homo sapiens 124-132 15932941-5 2005 A polyglutamine-expanded version of ataxin-7 assembles a SAGA complex that is depleted of critical proteins that regulate the ability of SAGA to acetylate nucleosomes. polyglutamine 2-15 ataxin 7 Homo sapiens 36-44 15932940-1 2005 Spinocerebellar ataxia type 7 (SCA7) is characterized by cone-rod dystrophy retinal degeneration and is caused by a polyglutamine [poly(Q)] expansion within ataxin-7, a protein of previously unknown function. polyglutamine 116-129 ataxin 7 Homo sapiens 0-29 15932940-1 2005 Spinocerebellar ataxia type 7 (SCA7) is characterized by cone-rod dystrophy retinal degeneration and is caused by a polyglutamine [poly(Q)] expansion within ataxin-7, a protein of previously unknown function. polyglutamine 116-129 ataxin 7 Homo sapiens 31-35 15932940-1 2005 Spinocerebellar ataxia type 7 (SCA7) is characterized by cone-rod dystrophy retinal degeneration and is caused by a polyglutamine [poly(Q)] expansion within ataxin-7, a protein of previously unknown function. polyglutamine 116-129 ataxin 7 Homo sapiens 157-165 15932940-1 2005 Spinocerebellar ataxia type 7 (SCA7) is characterized by cone-rod dystrophy retinal degeneration and is caused by a polyglutamine [poly(Q)] expansion within ataxin-7, a protein of previously unknown function. polyglutamine 131-138 ataxin 7 Homo sapiens 0-29 15932940-1 2005 Spinocerebellar ataxia type 7 (SCA7) is characterized by cone-rod dystrophy retinal degeneration and is caused by a polyglutamine [poly(Q)] expansion within ataxin-7, a protein of previously unknown function. polyglutamine 131-138 ataxin 7 Homo sapiens 31-35 15932940-1 2005 Spinocerebellar ataxia type 7 (SCA7) is characterized by cone-rod dystrophy retinal degeneration and is caused by a polyglutamine [poly(Q)] expansion within ataxin-7, a protein of previously unknown function. polyglutamine 131-138 ataxin 7 Homo sapiens 157-165 15895563-2 2005 The translated proteins contain abnormally long polyglutamine stretches, and SCA-1, SCA-2, SCA-3/Machado-Joseph disease (MJD), SCA-6, SCA-7, and SCA-17 are "polyglutamine diseases". polyglutamine 157-170 ataxin 7 Homo sapiens 134-139 15895563-2 2005 The translated proteins contain abnormally long polyglutamine stretches, and SCA-1, SCA-2, SCA-3/Machado-Joseph disease (MJD), SCA-6, SCA-7, and SCA-17 are "polyglutamine diseases". polyglutamine 157-170 ataxin 7 Homo sapiens 145-151 14571264-2 2004 The disease is caused by expansion of a CAG trinucleotide repeat within the SCA7 gene, which encodes a polyglutamine tract within a novel protein, termed ataxin-7. polyglutamine 103-116 ataxin 7 Homo sapiens 76-80 15115762-1 2004 Spinocerebellar ataxia type 7 (SCA7) is a neurodegenerative disorder caused by a CAG repeat expansion in the SCA7 gene leading to elongation of a polyglutamine tract in ataxin-7, a protein of unknown function. polyglutamine 146-159 ataxin 7 Homo sapiens 0-29 15115762-1 2004 Spinocerebellar ataxia type 7 (SCA7) is a neurodegenerative disorder caused by a CAG repeat expansion in the SCA7 gene leading to elongation of a polyglutamine tract in ataxin-7, a protein of unknown function. polyglutamine 146-159 ataxin 7 Homo sapiens 31-35 15115762-1 2004 Spinocerebellar ataxia type 7 (SCA7) is a neurodegenerative disorder caused by a CAG repeat expansion in the SCA7 gene leading to elongation of a polyglutamine tract in ataxin-7, a protein of unknown function. polyglutamine 146-159 ataxin 7 Homo sapiens 109-113 15115762-1 2004 Spinocerebellar ataxia type 7 (SCA7) is a neurodegenerative disorder caused by a CAG repeat expansion in the SCA7 gene leading to elongation of a polyglutamine tract in ataxin-7, a protein of unknown function. polyglutamine 146-159 ataxin 7 Homo sapiens 169-177 15115762-7 2004 Finally, polyglutamine expansion in ataxin-7 did not affect its incorporation into TFTC/STAGA complexes purified from SCA7 patient cells. polyglutamine 9-22 ataxin 7 Homo sapiens 36-44 14571264-2 2004 The disease is caused by expansion of a CAG trinucleotide repeat within the SCA7 gene, which encodes a polyglutamine tract within a novel protein, termed ataxin-7. polyglutamine 103-116 ataxin 7 Homo sapiens 154-162 14571264-3 2004 The expansion of polyglutamine-encoding CAG repeats in dissimilar genes underlies eight neurodegenerative conditions besides SCA7, including a number of dominant ataxias related to SCA7. polyglutamine 17-30 ataxin 7 Homo sapiens 125-129 14571264-3 2004 The expansion of polyglutamine-encoding CAG repeats in dissimilar genes underlies eight neurodegenerative conditions besides SCA7, including a number of dominant ataxias related to SCA7. polyglutamine 17-30 ataxin 7 Homo sapiens 181-185 14613968-1 2004 Spinocerebellar ataxia type 7 (SCA7) is an inherited neurodegenerative disorder caused by expansion of a polyglutamine tract in the ataxin-7 protein. polyglutamine 105-118 ataxin 7 Homo sapiens 0-29 14613968-1 2004 Spinocerebellar ataxia type 7 (SCA7) is an inherited neurodegenerative disorder caused by expansion of a polyglutamine tract in the ataxin-7 protein. polyglutamine 105-118 ataxin 7 Homo sapiens 31-35 14613968-1 2004 Spinocerebellar ataxia type 7 (SCA7) is an inherited neurodegenerative disorder caused by expansion of a polyglutamine tract in the ataxin-7 protein. polyglutamine 105-118 ataxin 7 Homo sapiens 132-140 12533095-1 2003 CONTEXT: Polyglutamine-mediated neurodegeneration in spinocerebellar ataxia type 7 (SCA7) involves specific central nervous system structures despite widespread expression of the mutant ataxin-7 protein. polyglutamine 9-22 ataxin 7 Homo sapiens 84-88 12699716-2 2003 Within such a scheme of progressive expansion of polyglutamine stretches in strict parallel correlation with increased CAG trinucleotide repeats in genes such as ataxin-7 and its messenger RNA, it would appear that a fundamental relationship of accumulation directly inducing biophysical disruption between nuclear/nucleolar and cytoplasmic protein machineries would constitute a dysfunctional dysequilibrium accounting for self-progressive neuronal degeneration with atrophy of the cerebral cortex and ganglia such as the caudate, that is limited often to specific population groups of neurons. polyglutamine 49-62 ataxin 7 Homo sapiens 162-170 12758065-1 2003 Recently, an inherited spinocerebellar ataxia (SCA17) has been attributed to polyglutamine coding expansions within the gene coding for human TATA-box binding protein (TBP). polyglutamine 77-90 ataxin 7 Homo sapiens 47-52 12533095-1 2003 CONTEXT: Polyglutamine-mediated neurodegeneration in spinocerebellar ataxia type 7 (SCA7) involves specific central nervous system structures despite widespread expression of the mutant ataxin-7 protein. polyglutamine 9-22 ataxin 7 Homo sapiens 186-194 12533095-5 2003 CONCLUSIONS: In addition to expanding our understanding of SCA7 gene expression, identification of a novel ataxin-7 protein enriched in the central nervous system suggests that expression of multiple polyglutamine-containing proteins may play a role in generating the neurodegenerative patterns characteristic of SCA7 and other polyglutamine expansion diseases. polyglutamine 200-213 ataxin 7 Homo sapiens 107-115 12533095-5 2003 CONCLUSIONS: In addition to expanding our understanding of SCA7 gene expression, identification of a novel ataxin-7 protein enriched in the central nervous system suggests that expression of multiple polyglutamine-containing proteins may play a role in generating the neurodegenerative patterns characteristic of SCA7 and other polyglutamine expansion diseases. polyglutamine 200-213 ataxin 7 Homo sapiens 313-317 12533095-5 2003 CONCLUSIONS: In addition to expanding our understanding of SCA7 gene expression, identification of a novel ataxin-7 protein enriched in the central nervous system suggests that expression of multiple polyglutamine-containing proteins may play a role in generating the neurodegenerative patterns characteristic of SCA7 and other polyglutamine expansion diseases. polyglutamine 328-341 ataxin 7 Homo sapiens 107-115 12235815-0 2001 [SCA17, a novel polyglutamine disease caused by the expansion of polyglutamine tracts in TATA-binding protein]. polyglutamine 16-29 ataxin 7 Homo sapiens 1-6 14526176-5 2003 SCA7 has a number of features in common with other diseases with polyglutamine expansions: (i) the appearance of clinical symptoms above a threshold number of CAG repeats (>35); (ii) a correlation between the size of the expansion and the rate of progression of the disease: the larger the repeat, the faster the progression; (iii) instability of the repeat sequence (approximately 12 CAG/transmission) that accounts for the marked anticipation of approximately 20 years/generation. polyglutamine 65-78 ataxin 7 Homo sapiens 0-4 12490531-2 2003 In humans, SCA7 is characterized by marked anticipation due to intergenerational repeat instability with a bias toward expansion, and is thus regarded as the most unstable of the polyglutamine diseases. polyglutamine 179-192 ataxin 7 Homo sapiens 11-15 12070661-2 2002 The disease is caused by an expanded polyglutamine tract in the protein ataxin-7. polyglutamine 37-50 ataxin 7 Homo sapiens 72-80 12077003-1 2002 Spinocerebellar ataxia type 7 (SCA7) is a hereditary progressive cerebellar ataxia with retinal degeneration associated with an abnormally expanded polyglutamine stretch. polyglutamine 148-161 ataxin 7 Homo sapiens 0-29 12077003-1 2002 Spinocerebellar ataxia type 7 (SCA7) is a hereditary progressive cerebellar ataxia with retinal degeneration associated with an abnormally expanded polyglutamine stretch. polyglutamine 148-161 ataxin 7 Homo sapiens 31-35 11354830-9 2001 This study broadens the current understanding of ataxin-7 localization and incorporates for the first time analysis of late-onset SCA7 patients where polyglutamine tract lengths are relatively shorter and disease course less severe than in previously described infantile-onset cases. polyglutamine 150-163 ataxin 7 Homo sapiens 130-134 11448935-0 2001 SCA17, a novel autosomal dominant cerebellar ataxia caused by an expanded polyglutamine in TATA-binding protein. polyglutamine 74-87 ataxin 7 Homo sapiens 0-5 11719247-5 2001 Recently, the transglutaminase activity has been hypothesized to be involved in the pathogenetic mechanisms responsible for the formation of cellular inclusions present in Huntington disease and in all the other polyglutamine (polyQ) diseases hitherto identified, such as spinobulbar muscular atrophy or Kennedy disease, spinocerebellar ataxias (SCA-1, SCA-2, SCA-3 or Machado-Joseph disease, SCA-6 and SCA-7) and dentatorubropallidoluysian atrophy. polyglutamine 227-232 ataxin 7 Homo sapiens 403-408 10970064-5 2000 The mutations that cause SCA1, SCA2, SCA3, SCA6 and SCA7 share the common feature of an expanded CAG sequence, encoding an abnormally long polyglutamine tract within the respective gene products. polyglutamine 139-152 ataxin 7 Homo sapiens 52-56 10841760-3 2000 The SCA7 gene product, ataxin-7, is an 897 amino acid protein with an expandable polyglutamine tract close to its N-terminus. polyglutamine 81-94 ataxin 7 Homo sapiens 4-8 10885657-2 2000 The expansion is translated into an extended polyglutamine stretch in the protein ataxin-7, a protein of unknown function. polyglutamine 45-58 ataxin 7 Homo sapiens 82-90 10928570-4 2000 The first type of mutation present in SCA1, SCA2, SCA3, and SCA7 is an expanded CAG repeat in genes of unknown function that are translated into proteins with expanded polyglutamine tracts. polyglutamine 168-181 ataxin 7 Homo sapiens 60-64 10841760-3 2000 The SCA7 gene product, ataxin-7, is an 897 amino acid protein with an expandable polyglutamine tract close to its N-terminus. polyglutamine 81-94 ataxin 7 Homo sapiens 23-31 34906452-0 2022 Digenic inheritance of STUB1 variants and TBP polyglutamine expansions explains the incomplete penetrance of SCA17 and SCA48. polyglutamine 46-59 ataxin 7 Homo sapiens 109-114 10712199-2 2000 The mutant proteins have shown an expanded polyglutamine tract in SCA1, SCA2, MJD/SCA3, SCA6, SCA7, and DRPLA; a glycine-to-arginine substitution was found in SCA6 as well. polyglutamine 43-56 ataxin 7 Homo sapiens 94-98 10640674-2 1999 The spinocerebellar ataxia type 7 (SCA7) is associated with pigmentary macular dystrophy and retinal degeneration leading to blindness caused by a CAG/polyglutamine (polyGln) expansion in the coding region of the SCA7 gene/protein. polyglutamine 151-164 ataxin 7 Homo sapiens 4-33 10640674-2 1999 The spinocerebellar ataxia type 7 (SCA7) is associated with pigmentary macular dystrophy and retinal degeneration leading to blindness caused by a CAG/polyglutamine (polyGln) expansion in the coding region of the SCA7 gene/protein. polyglutamine 151-164 ataxin 7 Homo sapiens 35-39 34906452-1 2022 PURPOSE: This study aimed to unravel the genetic factors underlying missing heritability in spinocerebellar ataxia type 17 (SCA17) caused by polyglutamine-encoding CAG/CAA repeat expansions in the TBP gene. polyglutamine 141-154 ataxin 7 Homo sapiens 124-129 33338633-0 2021 Polyglutamine expanded Ataxin-7 induces DNA damage and alters FUS localization and function. polyglutamine 0-13 ataxin 7 Homo sapiens 23-31 35422034-1 2022 CAG-expanded ATXN7 has been previously defined in the pathogenesis of spinocerebellar ataxia type 7 (SCA7), a polyglutamine expansion autosomal dominant cerebellar ataxia. polyglutamine 110-123 ataxin 7 Homo sapiens 70-99 35422034-1 2022 CAG-expanded ATXN7 has been previously defined in the pathogenesis of spinocerebellar ataxia type 7 (SCA7), a polyglutamine expansion autosomal dominant cerebellar ataxia. polyglutamine 110-123 ataxin 7 Homo sapiens 101-105 35401096-1 2022 Spinocerebellar ataxia (SCA) type 7 (SCA7) is caused by a CAG trinucleotide repeat expansion in the ataxin 7 (ATXN7) gene, which results in polyglutamine expansion at the amino terminus of the ATXN7 protein. polyglutamine 140-153 ataxin 7 Homo sapiens 37-41 35401096-1 2022 Spinocerebellar ataxia (SCA) type 7 (SCA7) is caused by a CAG trinucleotide repeat expansion in the ataxin 7 (ATXN7) gene, which results in polyglutamine expansion at the amino terminus of the ATXN7 protein. polyglutamine 140-153 ataxin 7 Homo sapiens 100-108 35401096-1 2022 Spinocerebellar ataxia (SCA) type 7 (SCA7) is caused by a CAG trinucleotide repeat expansion in the ataxin 7 (ATXN7) gene, which results in polyglutamine expansion at the amino terminus of the ATXN7 protein. polyglutamine 140-153 ataxin 7 Homo sapiens 110-115 35401096-1 2022 Spinocerebellar ataxia (SCA) type 7 (SCA7) is caused by a CAG trinucleotide repeat expansion in the ataxin 7 (ATXN7) gene, which results in polyglutamine expansion at the amino terminus of the ATXN7 protein. polyglutamine 140-153 ataxin 7 Homo sapiens 193-198 33837238-3 2021 Here, we took the fragments of polyQ-expanded (PQE) ataxin-7 (Atx7) and huntingtin (Htt) as models to investigate the effect of polyQ aggregates on the cellular proteostasis of endogenous ataxin-3 (Atx3), a protein that frequently appears in diverse inclusion bodies. polyglutamine 31-36 ataxin 7 Homo sapiens 52-60 33626063-1 2021 Spinocerebellar ataxia type 7 (SCA7) is an inherited neurodegenerative disease caused by a polyglutamine repeat expansion in the ATXN7 gene. polyglutamine 91-104 ataxin 7 Homo sapiens 0-29 33626063-1 2021 Spinocerebellar ataxia type 7 (SCA7) is an inherited neurodegenerative disease caused by a polyglutamine repeat expansion in the ATXN7 gene. polyglutamine 91-104 ataxin 7 Homo sapiens 31-35 33626063-1 2021 Spinocerebellar ataxia type 7 (SCA7) is an inherited neurodegenerative disease caused by a polyglutamine repeat expansion in the ATXN7 gene. polyglutamine 91-104 ataxin 7 Homo sapiens 129-134 33338633-1 2021 Polyglutamine (polyQ) diseases, such as Spinocerebellar ataxia type 7 (SCA7), are caused by expansions of polyQ repeats in disease specific proteins. polyglutamine 0-13 ataxin 7 Homo sapiens 40-69 33338633-1 2021 Polyglutamine (polyQ) diseases, such as Spinocerebellar ataxia type 7 (SCA7), are caused by expansions of polyQ repeats in disease specific proteins. polyglutamine 0-13 ataxin 7 Homo sapiens 71-75 33338633-1 2021 Polyglutamine (polyQ) diseases, such as Spinocerebellar ataxia type 7 (SCA7), are caused by expansions of polyQ repeats in disease specific proteins. polyglutamine 15-20 ataxin 7 Homo sapiens 40-69 33338633-1 2021 Polyglutamine (polyQ) diseases, such as Spinocerebellar ataxia type 7 (SCA7), are caused by expansions of polyQ repeats in disease specific proteins. polyglutamine 15-20 ataxin 7 Homo sapiens 71-75 33338633-1 2021 Polyglutamine (polyQ) diseases, such as Spinocerebellar ataxia type 7 (SCA7), are caused by expansions of polyQ repeats in disease specific proteins. polyglutamine 106-111 ataxin 7 Homo sapiens 40-69 33338633-1 2021 Polyglutamine (polyQ) diseases, such as Spinocerebellar ataxia type 7 (SCA7), are caused by expansions of polyQ repeats in disease specific proteins. polyglutamine 106-111 ataxin 7 Homo sapiens 71-75 31432449-2 2019 SCA7 is due to the expansion of a CAG triplet repeat that is translated into a polyglutamine tract in ATXN7. polyglutamine 79-92 ataxin 7 Homo sapiens 0-4 32962458-1 2020 INTRODUCTION: Six of the most frequent dominantly inherited spinocerebellar ataxias (SCAs) worldwide - SCA1, SCA2, SCA3, SCA6, SCA7, and SCA17 - are caused by an expansion of a polyglutamine (polyQ) tract in the corresponding proteins. polyglutamine 177-190 ataxin 7 Homo sapiens 127-131 32962458-1 2020 INTRODUCTION: Six of the most frequent dominantly inherited spinocerebellar ataxias (SCAs) worldwide - SCA1, SCA2, SCA3, SCA6, SCA7, and SCA17 - are caused by an expansion of a polyglutamine (polyQ) tract in the corresponding proteins. polyglutamine 177-190 ataxin 7 Homo sapiens 137-142 32962458-1 2020 INTRODUCTION: Six of the most frequent dominantly inherited spinocerebellar ataxias (SCAs) worldwide - SCA1, SCA2, SCA3, SCA6, SCA7, and SCA17 - are caused by an expansion of a polyglutamine (polyQ) tract in the corresponding proteins. polyglutamine 192-197 ataxin 7 Homo sapiens 127-131 32962458-1 2020 INTRODUCTION: Six of the most frequent dominantly inherited spinocerebellar ataxias (SCAs) worldwide - SCA1, SCA2, SCA3, SCA6, SCA7, and SCA17 - are caused by an expansion of a polyglutamine (polyQ) tract in the corresponding proteins. polyglutamine 192-197 ataxin 7 Homo sapiens 137-142 32581696-1 2020 Polyglutamine spinocerebellar ataxias (polyQ SCAs) include SCA1, SCA2, SCA3, SCA6, SCA7, and SCA17 and constitute a group of adult onset neurodegenerative disorders caused by the expansion of a CAG repeat sequence located within the coding region of specific genes, which translates into polyglutamine tract in the corresponding proteins. polyglutamine 0-13 ataxin 7 Homo sapiens 83-87 32581696-1 2020 Polyglutamine spinocerebellar ataxias (polyQ SCAs) include SCA1, SCA2, SCA3, SCA6, SCA7, and SCA17 and constitute a group of adult onset neurodegenerative disorders caused by the expansion of a CAG repeat sequence located within the coding region of specific genes, which translates into polyglutamine tract in the corresponding proteins. polyglutamine 0-13 ataxin 7 Homo sapiens 93-98 32581673-2 2020 These polyQ SCAs (SCA1, SCA2, SCA3, SCA6, SCA7, and SCA17) are inherited neurodegenerative diseases characterized by the progressive atrophy of the cerebellum and connected regions of the nervous system, which leads to loss of fine muscle movement coordination. polyglutamine 6-11 ataxin 7 Homo sapiens 42-46 32581673-2 2020 These polyQ SCAs (SCA1, SCA2, SCA3, SCA6, SCA7, and SCA17) are inherited neurodegenerative diseases characterized by the progressive atrophy of the cerebellum and connected regions of the nervous system, which leads to loss of fine muscle movement coordination. polyglutamine 6-11 ataxin 7 Homo sapiens 52-57 31927329-4 2020 Here we show that repeat-targeting short hairpin RNAs preferentially reduce the levels of mutant huntingtin, atrophin-1, ataxin-3, and ataxin-7 proteins in patient-derived fibroblasts and may serve as universal allele-selective reagents for polyglutamine (polyQ) diseases. polyglutamine 241-254 ataxin 7 Homo sapiens 135-143 31927329-4 2020 Here we show that repeat-targeting short hairpin RNAs preferentially reduce the levels of mutant huntingtin, atrophin-1, ataxin-3, and ataxin-7 proteins in patient-derived fibroblasts and may serve as universal allele-selective reagents for polyglutamine (polyQ) diseases. polyglutamine 256-261 ataxin 7 Homo sapiens 135-143 31317427-1 2019 Spinocerebellar ataxia type 17 (SCA17) is caused by polyglutamine (polyQ) expansion in the TATA box-binding protein (TBP), which functions as a general transcription factor. polyglutamine 52-65 ataxin 7 Homo sapiens 0-30 31317427-1 2019 Spinocerebellar ataxia type 17 (SCA17) is caused by polyglutamine (polyQ) expansion in the TATA box-binding protein (TBP), which functions as a general transcription factor. polyglutamine 52-65 ataxin 7 Homo sapiens 32-37 31317427-1 2019 Spinocerebellar ataxia type 17 (SCA17) is caused by polyglutamine (polyQ) expansion in the TATA box-binding protein (TBP), which functions as a general transcription factor. polyglutamine 67-72 ataxin 7 Homo sapiens 0-30 31317427-1 2019 Spinocerebellar ataxia type 17 (SCA17) is caused by polyglutamine (polyQ) expansion in the TATA box-binding protein (TBP), which functions as a general transcription factor. polyglutamine 67-72 ataxin 7 Homo sapiens 32-37 31317427-2 2019 Like other polyQ expansion-mediated diseases, SCA17 is characterized by late-onset and selective neurodegeneration, despite the disease protein being ubiquitously expressed in the body. polyglutamine 11-16 ataxin 7 Homo sapiens 46-51 31317427-4 2019 The well-characterized function of TBP and typical neurodegeneration in SCA17 give us opportunities to understand how polyQ expansion causes selective neurodegeneration and to develop effective therapeutics. polyglutamine 118-123 ataxin 7 Homo sapiens 72-77 32518289-0 2020 Author Correction: Structural and dynamic studies reveal that the Ala-rich region of ataxin-7 initiates alpha-helix formation of the polyQ tract but suppresses its aggregation. polyglutamine 133-138 ataxin 7 Homo sapiens 85-93 31767406-3 2020 Here, we demonstrate that the same agents also deplete other polyglutamine disease-related proteins: mutant ataxin-3 and ataxin-7 in cells from spino-cerebellar ataxia patients, and mutant atrophin-1 in cells from dentatorubral-pallidoluysian atrophy patients. polyglutamine 61-74 ataxin 7 Homo sapiens 121-129 31432449-2 2019 SCA7 is due to the expansion of a CAG triplet repeat that is translated into a polyglutamine tract in ATXN7. polyglutamine 79-92 ataxin 7 Homo sapiens 102-107 31432449-6 2019 Polyglutamine expansion in ATXN7 causes its misfolding and intranuclear accumulation, leading to changes in interactions with native partners and/or partners sequestration in insoluble nuclear inclusions. polyglutamine 0-13 ataxin 7 Homo sapiens 27-32 31348003-1 2019 Atxn7, a subunit of SAGA chromatin remodeling complex, is subject to polyglutamine expansion at the amino terminus, causing spinocerebellar ataxia type 7 (SCA7), a progressive retinal and neurodegenerative disease. polyglutamine 69-82 ataxin 7 Homo sapiens 0-5 31348003-1 2019 Atxn7, a subunit of SAGA chromatin remodeling complex, is subject to polyglutamine expansion at the amino terminus, causing spinocerebellar ataxia type 7 (SCA7), a progressive retinal and neurodegenerative disease. polyglutamine 69-82 ataxin 7 Homo sapiens 124-153 31348003-1 2019 Atxn7, a subunit of SAGA chromatin remodeling complex, is subject to polyglutamine expansion at the amino terminus, causing spinocerebellar ataxia type 7 (SCA7), a progressive retinal and neurodegenerative disease. polyglutamine 69-82 ataxin 7 Homo sapiens 155-159 30707359-7 2019 We show its usefulness by performing a comparative study of the interactome of the nine polyglutamine (polyQ) disease proteins, namely androgen receptor (AR), atrophin-1 (ATN1), ataxin 1 (ATXN1), ataxin 2 (ATXN2), ataxin 3 (ATXN3), ataxin 7 (ATXN7), calcium voltage-gated channel subunit alpha1 A (CACNA1A), Huntingtin (HTT), and TATA-binding protein (TBP). polyglutamine 88-101 ataxin 7 Homo sapiens 232-240 31097749-0 2019 Structural and dynamic studies reveal that the Ala-rich region of ataxin-7 initiates alpha-helix formation of the polyQ tract but suppresses its aggregation. polyglutamine 114-119 ataxin 7 Homo sapiens 66-74 31097749-6 2019 The ARR alpha-helix can initiate and stabilize helical formation of the following polyQ tract, but it may suppress aggregation of the polyQ-expanded Atx7-N both in vitro and in cell. polyglutamine 134-139 ataxin 7 Homo sapiens 149-155 31097749-7 2019 Thus, the preceding ARR segment in Atx7-N may influence the dynamic structure and aggregation property of the polyQ tract and even determine the threshold of the pathogenic polyQ lengths. polyglutamine 110-115 ataxin 7 Homo sapiens 35-41 30707359-7 2019 We show its usefulness by performing a comparative study of the interactome of the nine polyglutamine (polyQ) disease proteins, namely androgen receptor (AR), atrophin-1 (ATN1), ataxin 1 (ATXN1), ataxin 2 (ATXN2), ataxin 3 (ATXN3), ataxin 7 (ATXN7), calcium voltage-gated channel subunit alpha1 A (CACNA1A), Huntingtin (HTT), and TATA-binding protein (TBP). polyglutamine 88-101 ataxin 7 Homo sapiens 242-247 30699348-1 2019 Spinocerebellar ataxia type 7 (SCA7) is a retinal-cerebellar degenerative disorder caused by CAG-polyglutamine (polyQ) repeat expansions in the ataxin-7 gene. polyglutamine 112-117 ataxin 7 Homo sapiens 0-29 30699348-1 2019 Spinocerebellar ataxia type 7 (SCA7) is a retinal-cerebellar degenerative disorder caused by CAG-polyglutamine (polyQ) repeat expansions in the ataxin-7 gene. polyglutamine 112-117 ataxin 7 Homo sapiens 31-35 30699348-1 2019 Spinocerebellar ataxia type 7 (SCA7) is a retinal-cerebellar degenerative disorder caused by CAG-polyglutamine (polyQ) repeat expansions in the ataxin-7 gene. polyglutamine 112-117 ataxin 7 Homo sapiens 144-152 30473770-3 2018 Polyglutamine (polyQ) expansion diseases ( ATXN1/SCA1, ATXN2/SCA2, ATXN3/SCA3, CACNA1A/SCA6, ATXN7/SCA7, TBP/SCA17, and ATN1/DRPLA) are the most common group of SCAs. polyglutamine 0-13 ataxin 7 Homo sapiens 93-98 30559154-3 2019 Here, we show that endogenous ATXN7 is modified by SUMO proteins, thus also suggesting a physiological role for this modification under conditions of proteotoxic stress caused by the accumulation of polyQ-ATXN7. polyglutamine 199-204 ataxin 7 Homo sapiens 30-35 30559154-3 2019 Here, we show that endogenous ATXN7 is modified by SUMO proteins, thus also suggesting a physiological role for this modification under conditions of proteotoxic stress caused by the accumulation of polyQ-ATXN7. polyglutamine 199-204 ataxin 7 Homo sapiens 205-210 30559154-4 2019 Co-immunoprecipitation experiments, immunofluorescence microscopy and proximity ligation assays confirmed the colocalization and interaction of polyQ-ATXN7 with SUMO2 in cells. polyglutamine 144-149 ataxin 7 Homo sapiens 150-155 30559154-6 2019 Overexpression of RNF4 and/or SUMO2 significantly decreased levels of polyQ-ATXN7 and, upon proteasomal inhibition, led to a marked increase in the polyubiquitination of polyQ-ATXN7. polyglutamine 70-75 ataxin 7 Homo sapiens 76-81 30559154-6 2019 Overexpression of RNF4 and/or SUMO2 significantly decreased levels of polyQ-ATXN7 and, upon proteasomal inhibition, led to a marked increase in the polyubiquitination of polyQ-ATXN7. polyglutamine 170-175 ataxin 7 Homo sapiens 76-81 30559154-6 2019 Overexpression of RNF4 and/or SUMO2 significantly decreased levels of polyQ-ATXN7 and, upon proteasomal inhibition, led to a marked increase in the polyubiquitination of polyQ-ATXN7. polyglutamine 170-175 ataxin 7 Homo sapiens 176-181 30559154-7 2019 This provides a mechanism for the clearance of polyQ-ATXN7 from affected cells that involves the recruitment of RNF4 by SUMO2/3-modified polyQ-ATXN7, thus leading to its ubiquitination and proteasomal degradation. polyglutamine 47-52 ataxin 7 Homo sapiens 53-58 30559154-7 2019 This provides a mechanism for the clearance of polyQ-ATXN7 from affected cells that involves the recruitment of RNF4 by SUMO2/3-modified polyQ-ATXN7, thus leading to its ubiquitination and proteasomal degradation. polyglutamine 47-52 ataxin 7 Homo sapiens 143-148 30559154-7 2019 This provides a mechanism for the clearance of polyQ-ATXN7 from affected cells that involves the recruitment of RNF4 by SUMO2/3-modified polyQ-ATXN7, thus leading to its ubiquitination and proteasomal degradation. polyglutamine 137-142 ataxin 7 Homo sapiens 53-58 30559154-7 2019 This provides a mechanism for the clearance of polyQ-ATXN7 from affected cells that involves the recruitment of RNF4 by SUMO2/3-modified polyQ-ATXN7, thus leading to its ubiquitination and proteasomal degradation. polyglutamine 137-142 ataxin 7 Homo sapiens 143-148 30473770-3 2018 Polyglutamine (polyQ) expansion diseases ( ATXN1/SCA1, ATXN2/SCA2, ATXN3/SCA3, CACNA1A/SCA6, ATXN7/SCA7, TBP/SCA17, and ATN1/DRPLA) are the most common group of SCAs. polyglutamine 0-13 ataxin 7 Homo sapiens 99-103 30473770-3 2018 Polyglutamine (polyQ) expansion diseases ( ATXN1/SCA1, ATXN2/SCA2, ATXN3/SCA3, CACNA1A/SCA6, ATXN7/SCA7, TBP/SCA17, and ATN1/DRPLA) are the most common group of SCAs. polyglutamine 0-13 ataxin 7 Homo sapiens 109-114 30473770-3 2018 Polyglutamine (polyQ) expansion diseases ( ATXN1/SCA1, ATXN2/SCA2, ATXN3/SCA3, CACNA1A/SCA6, ATXN7/SCA7, TBP/SCA17, and ATN1/DRPLA) are the most common group of SCAs. polyglutamine 15-20 ataxin 7 Homo sapiens 99-103 29427104-4 2018 SCA7 is pathomechanistically related to the group of CAG/polyglutamine (polyQ) expansion disorders, which includes other SCAs (1-3, 6 and 17), Huntington"s disease, spinal bulbar muscular atrophy and dentatorubro pallidoluysian atrophy. polyglutamine 57-70 ataxin 7 Homo sapiens 0-4 29876803-1 2018 Spinocerebellar ataxia type 7 is a neurodegenerative inherited disease caused by a CAG expansion in the coding region of the ATXN7 gene, which results in the synthesis of polyglutamine-containing ataxin-7. polyglutamine 171-184 ataxin 7 Homo sapiens 125-130 29876803-1 2018 Spinocerebellar ataxia type 7 is a neurodegenerative inherited disease caused by a CAG expansion in the coding region of the ATXN7 gene, which results in the synthesis of polyglutamine-containing ataxin-7. polyglutamine 171-184 ataxin 7 Homo sapiens 196-204 29427104-4 2018 SCA7 is pathomechanistically related to the group of CAG/polyglutamine (polyQ) expansion disorders, which includes other SCAs (1-3, 6 and 17), Huntington"s disease, spinal bulbar muscular atrophy and dentatorubro pallidoluysian atrophy. polyglutamine 72-77 ataxin 7 Homo sapiens 0-4 29427104-6 2018 The pathology is caused by an unstable CAG repeat expansion coding for a polyQ stretch in Ataxin-7 (ATXN7). polyglutamine 73-78 ataxin 7 Homo sapiens 90-98 29427104-6 2018 The pathology is caused by an unstable CAG repeat expansion coding for a polyQ stretch in Ataxin-7 (ATXN7). polyglutamine 73-78 ataxin 7 Homo sapiens 100-105 29427104-7 2018 PolyQ expansion in ATXN7 confers toxic properties and leads to selective neuronal degeneration in the cerebellum, the brain stem and the retina. polyglutamine 0-5 ataxin 7 Homo sapiens 19-24 28821675-1 2017 Spinocerebellar ataxia 17 (SCA17) is caused by polyglutamine (polyQ) repeat expansion in the TATA-binding protein (TBP) and is among a family of neurodegenerative diseases in which polyQ expansion leads to preferential neuronal loss in the brain. polyglutamine 47-60 ataxin 7 Homo sapiens 27-32 28821675-1 2017 Spinocerebellar ataxia 17 (SCA17) is caused by polyglutamine (polyQ) repeat expansion in the TATA-binding protein (TBP) and is among a family of neurodegenerative diseases in which polyQ expansion leads to preferential neuronal loss in the brain. polyglutamine 62-67 ataxin 7 Homo sapiens 27-32 28821675-1 2017 Spinocerebellar ataxia 17 (SCA17) is caused by polyglutamine (polyQ) repeat expansion in the TATA-binding protein (TBP) and is among a family of neurodegenerative diseases in which polyQ expansion leads to preferential neuronal loss in the brain. polyglutamine 181-186 ataxin 7 Homo sapiens 27-32 28821675-8 2017 Our results indicate that the synergistic toxicity of mutant TBP in neuronal and glial cells plays a critical role in SCA17 pathogenesis and that targeting glial inflammation could be a potential therapeutic approach for SCA17 treatment.SIGNIFICANCE STATEMENT Mutant TBP with polyglutamine expansion preferentially affects neuronal viability in SCA17 patients. polyglutamine 276-289 ataxin 7 Homo sapiens 221-226 28821675-8 2017 Our results indicate that the synergistic toxicity of mutant TBP in neuronal and glial cells plays a critical role in SCA17 pathogenesis and that targeting glial inflammation could be a potential therapeutic approach for SCA17 treatment.SIGNIFICANCE STATEMENT Mutant TBP with polyglutamine expansion preferentially affects neuronal viability in SCA17 patients. polyglutamine 276-289 ataxin 7 Homo sapiens 221-226 28032013-1 2016 Spinocerebellar ataxia 17 (SCA17) belongs to the family of 9 genetically inherited, late-onset neurodegenerative diseases, which are caused by polyglutamine (polyQ) expansion in different proteins. polyglutamine 143-156 ataxin 7 Homo sapiens 0-25 28774347-2 2017 Expansion of a polyglutamine tract in the N-terminal of TBP is the causal mutation in SCA17. polyglutamine 15-28 ataxin 7 Homo sapiens 86-91 28774347-7 2017 METHODS: Gene expression profiling was performed subsequent to the expression of TBP containing polyglutamine in a cellular model of SCA17. polyglutamine 96-109 ataxin 7 Homo sapiens 133-138 28032013-1 2016 Spinocerebellar ataxia 17 (SCA17) belongs to the family of 9 genetically inherited, late-onset neurodegenerative diseases, which are caused by polyglutamine (polyQ) expansion in different proteins. polyglutamine 143-156 ataxin 7 Homo sapiens 27-32 28032013-1 2016 Spinocerebellar ataxia 17 (SCA17) belongs to the family of 9 genetically inherited, late-onset neurodegenerative diseases, which are caused by polyglutamine (polyQ) expansion in different proteins. polyglutamine 158-163 ataxin 7 Homo sapiens 0-25 28032013-1 2016 Spinocerebellar ataxia 17 (SCA17) belongs to the family of 9 genetically inherited, late-onset neurodegenerative diseases, which are caused by polyglutamine (polyQ) expansion in different proteins. polyglutamine 158-163 ataxin 7 Homo sapiens 27-32 25800379-6 2015 Using polyQ-mediated spinocerebellar ataxia type 17 (SCA17) cell and slice cultures, we found the aggregation was significantly prohibited by trehalose, lactulose, and melibiose, which may through up-regulating of autophagy. polyglutamine 6-11 ataxin 7 Homo sapiens 21-51 26195632-0 2015 Aggregation of Polyglutamine-expanded Ataxin 7 Protein Specifically Sequesters Ubiquitin-specific Protease 22 and Deteriorates Its Deubiquitinating Function in the Spt-Ada-Gcn5-Acetyltransferase (SAGA) Complex. polyglutamine 15-28 ataxin 7 Homo sapiens 38-46 26195632-1 2015 Human ataxin 7 (Atx7) is a component of the deubiquitination module (DUBm) in the Spt-Ada-Gcn5-acetyltransferase (SAGA) complex for transcriptional regulation, and expansion of its polyglutamine (polyQ) tract leads to spinocerebellar ataxia type 7. polyglutamine 181-194 ataxin 7 Homo sapiens 6-14 26195632-1 2015 Human ataxin 7 (Atx7) is a component of the deubiquitination module (DUBm) in the Spt-Ada-Gcn5-acetyltransferase (SAGA) complex for transcriptional regulation, and expansion of its polyglutamine (polyQ) tract leads to spinocerebellar ataxia type 7. polyglutamine 181-194 ataxin 7 Homo sapiens 16-20 26195632-1 2015 Human ataxin 7 (Atx7) is a component of the deubiquitination module (DUBm) in the Spt-Ada-Gcn5-acetyltransferase (SAGA) complex for transcriptional regulation, and expansion of its polyglutamine (polyQ) tract leads to spinocerebellar ataxia type 7. polyglutamine 196-201 ataxin 7 Homo sapiens 6-14 26195632-1 2015 Human ataxin 7 (Atx7) is a component of the deubiquitination module (DUBm) in the Spt-Ada-Gcn5-acetyltransferase (SAGA) complex for transcriptional regulation, and expansion of its polyglutamine (polyQ) tract leads to spinocerebellar ataxia type 7. polyglutamine 196-201 ataxin 7 Homo sapiens 16-20 26195632-2 2015 However, how polyQ expansion of Atx7 affects DUBm function remains elusive. polyglutamine 13-18 ataxin 7 Homo sapiens 32-36 26195632-3 2015 We investigated the effects of polyQ-expanded Atx7 on ubiquitin-specific protease (USP22), an interacting partner of Atx7 functioning in deubiquitination of histone H2B. polyglutamine 31-36 ataxin 7 Homo sapiens 46-50 26195632-3 2015 We investigated the effects of polyQ-expanded Atx7 on ubiquitin-specific protease (USP22), an interacting partner of Atx7 functioning in deubiquitination of histone H2B. polyglutamine 31-36 ataxin 7 Homo sapiens 117-121 26195632-4 2015 The results showed that the inclusions or aggregates formed by polyQ-expanded Atx7 specifically sequester USP22 through their interactions mediated by the N-terminal zinc finger domain of Atx7. polyglutamine 63-68 ataxin 7 Homo sapiens 78-82 26195632-4 2015 The results showed that the inclusions or aggregates formed by polyQ-expanded Atx7 specifically sequester USP22 through their interactions mediated by the N-terminal zinc finger domain of Atx7. polyglutamine 63-68 ataxin 7 Homo sapiens 188-192 26195632-6 2015 Moreover, polyQ expansion of Atx7 decreases the deubiquitinating activity of USP22 and, consequently, increases the level of monoubiquitinated H2B. polyglutamine 10-15 ataxin 7 Homo sapiens 29-33 26195632-7 2015 Therefore, we propose that polyQ-expanded Atx7 forms insoluble aggregates that sequester USP22 into a catalytically inactive state, and then the impaired DUBm loses the function to deubiquitinate monoubiquitinated histone H2B or H2A. polyglutamine 27-32 ataxin 7 Homo sapiens 42-46 25800379-6 2015 Using polyQ-mediated spinocerebellar ataxia type 17 (SCA17) cell and slice cultures, we found the aggregation was significantly prohibited by trehalose, lactulose, and melibiose, which may through up-regulating of autophagy. polyglutamine 6-11 ataxin 7 Homo sapiens 53-58 25054097-2 2014 This elongated CAG tract results in an Ataxin-7 protein bearing an expanded polyglutamine (PolyQ) repeat. polyglutamine 76-89 ataxin 7 Homo sapiens 39-47 25647692-1 2015 Spinocerebellar ataxia type 7 (SCA7) is one of the nine neurodegenerative disorders caused by expanded polyglutamine (polyQ) domains. polyglutamine 103-116 ataxin 7 Homo sapiens 0-29 25647692-1 2015 Spinocerebellar ataxia type 7 (SCA7) is one of the nine neurodegenerative disorders caused by expanded polyglutamine (polyQ) domains. polyglutamine 103-116 ataxin 7 Homo sapiens 31-35 25647692-1 2015 Spinocerebellar ataxia type 7 (SCA7) is one of the nine neurodegenerative disorders caused by expanded polyglutamine (polyQ) domains. polyglutamine 118-123 ataxin 7 Homo sapiens 0-29 25647692-1 2015 Spinocerebellar ataxia type 7 (SCA7) is one of the nine neurodegenerative disorders caused by expanded polyglutamine (polyQ) domains. polyglutamine 118-123 ataxin 7 Homo sapiens 31-35 25342886-0 2014 Indole and synthetic derivative activate chaperone expression to reduce polyQ aggregation in SCA17 neuronal cell and slice culture models. polyglutamine 72-77 ataxin 7 Homo sapiens 93-98 25342886-1 2014 In spinocerebellar ataxia type 17 (SCA17), the expansion of a translated CAG repeat in the TATA box binding protein (TBP) gene results in a long polyglutamine (polyQ) tract in the TBP protein, leading to intracellular accumulation of aggregated TBP and cell death. polyglutamine 145-158 ataxin 7 Homo sapiens 35-40 25342886-1 2014 In spinocerebellar ataxia type 17 (SCA17), the expansion of a translated CAG repeat in the TATA box binding protein (TBP) gene results in a long polyglutamine (polyQ) tract in the TBP protein, leading to intracellular accumulation of aggregated TBP and cell death. polyglutamine 160-165 ataxin 7 Homo sapiens 35-40 25342886-6 2014 Our results demonstrate how indole and derivative NC001-8 reduce polyQ aggregation to support their therapeutic potentials in SCA17 treatment. polyglutamine 65-70 ataxin 7 Homo sapiens 126-131 25054097-2 2014 This elongated CAG tract results in an Ataxin-7 protein bearing an expanded polyglutamine (PolyQ) repeat. polyglutamine 91-96 ataxin 7 Homo sapiens 39-47 25054097-6 2014 Here we discuss recent insights into Ataxin-7 function and, considering these findings, propose a model for how polyglutamine expansion of Ataxin-7 may affect Ataxin-7 function to alter chromatin modifications and gene expression. polyglutamine 112-125 ataxin 7 Homo sapiens 37-45 25054097-6 2014 Here we discuss recent insights into Ataxin-7 function and, considering these findings, propose a model for how polyglutamine expansion of Ataxin-7 may affect Ataxin-7 function to alter chromatin modifications and gene expression. polyglutamine 112-125 ataxin 7 Homo sapiens 139-147 25054097-6 2014 Here we discuss recent insights into Ataxin-7 function and, considering these findings, propose a model for how polyglutamine expansion of Ataxin-7 may affect Ataxin-7 function to alter chromatin modifications and gene expression. polyglutamine 112-125 ataxin 7 Homo sapiens 139-147 23592174-1 2013 Spinocerebellar ataxia type 7 (SCA7) is one of nine neurodegenerative disorders caused by expanded polyglutamine domains. polyglutamine 99-112 ataxin 7 Homo sapiens 0-29 24129567-0 2013 Direct inhibition of Gcn5 protein catalytic activity by polyglutamine-expanded ataxin-7. polyglutamine 56-69 ataxin 7 Homo sapiens 79-87 24129567-1 2013 Spinocerebellar ataxia type 7 (SCA7) is a neurodegenerative disease caused by polyglutamine (polyQ) expansion within the N-terminal region of the ataxin-7 protein, a known subunit of the SAGA complex. polyglutamine 78-91 ataxin 7 Homo sapiens 0-29 24129567-1 2013 Spinocerebellar ataxia type 7 (SCA7) is a neurodegenerative disease caused by polyglutamine (polyQ) expansion within the N-terminal region of the ataxin-7 protein, a known subunit of the SAGA complex. polyglutamine 78-91 ataxin 7 Homo sapiens 31-35 24129567-1 2013 Spinocerebellar ataxia type 7 (SCA7) is a neurodegenerative disease caused by polyglutamine (polyQ) expansion within the N-terminal region of the ataxin-7 protein, a known subunit of the SAGA complex. polyglutamine 78-91 ataxin 7 Homo sapiens 146-154 24129567-1 2013 Spinocerebellar ataxia type 7 (SCA7) is a neurodegenerative disease caused by polyglutamine (polyQ) expansion within the N-terminal region of the ataxin-7 protein, a known subunit of the SAGA complex. polyglutamine 93-98 ataxin 7 Homo sapiens 0-29 24129567-1 2013 Spinocerebellar ataxia type 7 (SCA7) is a neurodegenerative disease caused by polyglutamine (polyQ) expansion within the N-terminal region of the ataxin-7 protein, a known subunit of the SAGA complex. polyglutamine 93-98 ataxin 7 Homo sapiens 31-35 24129567-1 2013 Spinocerebellar ataxia type 7 (SCA7) is a neurodegenerative disease caused by polyglutamine (polyQ) expansion within the N-terminal region of the ataxin-7 protein, a known subunit of the SAGA complex. polyglutamine 93-98 ataxin 7 Homo sapiens 146-154 24129567-3 2013 We sought to determine whether and how polyQ-expanded ataxin-7 affects SAGA catalytic activity. polyglutamine 39-44 ataxin 7 Homo sapiens 54-62 24129567-4 2013 Here, we determined that polyQ-expanded ataxin-7 directly bound the Gcn5 catalytic core of SAGA while in association with its regulatory proteins, Ada2 and Ada3. polyglutamine 25-30 ataxin 7 Homo sapiens 40-48 24129567-6 2013 However, Gcn5 occupancy at the GAL1 and GAL7 promoters was increased in these cells, revealing a dominant-negative phenotype of the polyQ-expanded ataxin-7-incorporated, catalytically inactive SAGA. polyglutamine 132-137 ataxin 7 Homo sapiens 147-155 23892081-1 2013 Ataxin-7 (Atx7) is a component of the nuclear transcription co-activator complex; its polyglutamine (polyQ) expansion may cause nuclear accumulation and recruit numerous proteins to the intranuclear inclusion bodies. polyglutamine 86-99 ataxin 7 Homo sapiens 0-8 23892081-1 2013 Ataxin-7 (Atx7) is a component of the nuclear transcription co-activator complex; its polyglutamine (polyQ) expansion may cause nuclear accumulation and recruit numerous proteins to the intranuclear inclusion bodies. polyglutamine 86-99 ataxin 7 Homo sapiens 10-14 23892081-1 2013 Ataxin-7 (Atx7) is a component of the nuclear transcription co-activator complex; its polyglutamine (polyQ) expansion may cause nuclear accumulation and recruit numerous proteins to the intranuclear inclusion bodies. polyglutamine 101-106 ataxin 7 Homo sapiens 0-8 23892081-1 2013 Ataxin-7 (Atx7) is a component of the nuclear transcription co-activator complex; its polyglutamine (polyQ) expansion may cause nuclear accumulation and recruit numerous proteins to the intranuclear inclusion bodies. polyglutamine 101-106 ataxin 7 Homo sapiens 10-14 23892081-5 2013 Microscopy imaging demonstrated that sequestration of R85FL by the polyQ-expanded Atx7 in cell is mediated by this specific SH3C-PRR interaction, which is implicated in the pathogenesis of spinocerebellar ataxia 7. polyglutamine 67-72 ataxin 7 Homo sapiens 82-86 23592174-1 2013 Spinocerebellar ataxia type 7 (SCA7) is one of nine neurodegenerative disorders caused by expanded polyglutamine domains. polyglutamine 99-112 ataxin 7 Homo sapiens 31-35